On the public citation graph

Structure-Function Study of a Plasmodium falciparum Hsp70 Using Three Dimensional Modelling and in Vitro Analyses

0 signed · 61 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4670632openalex-extracted
inferred← citeshttps://doi.org/10.1002/iub.1146openalex-snapshot
Cysteine‐capped gold nanoparticles suppress aggregation of proteins exposed to heat stress
inferred← citeshttps://doi.org/10.1002/prot.25600openalex-snapshot
Structural and biochemical characterization of Plasmodium falciparum Hsp70‐x reveals functional versatility of its C‐terminal EEVN motif
inferred← citeshttps://doi.org/10.1007/978-1-4939-1130-1_17openalex-snapshot
The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_3openalex-snapshot
The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_4openalex-snapshot
Role of the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum
inferred← citeshttps://doi.org/10.1007/978-3-030-78397-6_8openalex-snapshot
Bioprospecting for Novel Heat Shock Protein Modulators: The New Frontier for Antimalarial Drug Discovery?
inferred← citeshttps://doi.org/10.1007/978-3-319-17211-8_6openalex-snapshot
The Role of Heat Shock Protein 70 in Infection and Immunity
inferred← citeshttps://doi.org/10.1007/978-3-642-28175-4_4openalex-snapshot
Targeting Conserved Pathways as a Strategy for Novel Drug Development: Disabling the Cellular Stress Response
inferred← citeshttps://doi.org/10.1007/978-94-007-7438-4_10openalex-snapshot
Heat Shock Proteins as Targets for Novel Anti-Malarial Drugs
inferred← citeshttps://doi.org/10.1007/978-94-007-7438-4_3openalex-snapshot
The Role of Hsp70s in the Development and Pathogenicity of Plasmodium Species
inferred← citeshttps://doi.org/10.1007/978-94-007-7438-4_4openalex-snapshot
Role of the Hsp40 Family of Proteins in the Survival and Pathogenesis of the Malaria Parasite
inferred← citeshttps://doi.org/10.1007/s12192-010-0250-6openalex-snapshot
Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock
inferred← citeshttps://doi.org/10.1007/s12192-011-0299-xopenalex-snapshot
Characterisation of the Plasmodium falciparum Hsp70–Hsp90 organising protein (PfHop)
inferred← citeshttps://doi.org/10.1007/s12192-016-0678-4openalex-snapshot
Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
inferred← citeshttps://doi.org/10.1007/s12192-017-0797-6openalex-snapshot
Polymyxin B inhibits the chaperone activity of Plasmodium falciparum Hsp70
inferred← citeshttps://doi.org/10.1007/s12192-021-01212-6openalex-snapshot
Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1
inferred← citeshttps://doi.org/10.1007/s12192-023-01339-8openalex-snapshot
Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro
inferred← citeshttps://doi.org/10.1007/s12551-019-00563-wopenalex-snapshot
Comparative structure-function features of Hsp70s of Plasmodium falciparum and human origins
inferred← citeshttps://doi.org/10.1007/s12551-023-01127-9openalex-snapshot
The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2024.119824openalex-snapshot
Proteostasis is a key driver of the pathogenesis in Apicomplexa
inferred← citeshttps://doi.org/10.1016/j.bbapap.2010.08.007openalex-snapshot
Exploring the positional importance of aromatic residues and lysine in the interactions of peptides with the Plasmodium falciparum Hsp70-1
inferred← citeshttps://doi.org/10.1016/j.biocel.2015.02.008openalex-snapshot
PFB0595w is a Plasmodium falciparum J protein that co-localizes with PfHsp70-1 and can stimulate its in vitro ATP hydrolysis activity
inferred← citeshttps://doi.org/10.1016/j.bpc.2009.03.006openalex-snapshot
Hsp70-1 from Plasmodium falciparum: Protein stability, domain analysis and chaperone activity
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e29690openalex-snapshot
Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.03.056openalex-snapshot
Characterisation of a unique linker segment of the Plasmodium falciparum cytosol localised Hsp110 chaperone
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.128070openalex-snapshot
Insertion of GGMP repeat residues of Plasmodium falciparum Hsp70-1 in the lid of DnaK adversely impacts client recognition
inferred← citeshttps://doi.org/10.1016/j.pep.2011.01.005openalex-snapshot
Co-expression of the Plasmodium falciparum molecular chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI
inferred← citeshttps://doi.org/10.1016/j.toxlet.2014.02.027openalex-snapshot
Immunomodulatory activity of zinc peroxide (ZnO2) and titanium dioxide (TiO2) nanoparticles and their effects on DNA and protein integrity
inferred← citeshttps://doi.org/10.1017/s003118201300228xopenalex-snapshot
Plasmodial Hsp40 and Hsp70 chaperones: current and future perspectives
inferred← citeshttps://doi.org/10.1021/acs.biochem.5c00120openalex-snapshot
Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers
inferred← citeshttps://doi.org/10.1080/0035919x.2022.2144536openalex-snapshot
Exploring the application of ELISA and slot blot as utility protein–protein interaction analysis tools
inferred← citeshttps://doi.org/10.1080/07391102.2013.834849openalex-snapshot
Plasmodium falciparumHsp70-x: a heat shock protein at the host–parasite interface
inferred← citeshttps://doi.org/10.1080/22221751.2026.2686468openalex-snapshot
Extracellular vesicles participate in proteostasis and heat shock adaptation in Plasmodium falciparum
inferred← citeshttps://doi.org/10.1111/j.1574-695x.2009.00639.xopenalex-snapshot
Plasmodial heat shock proteins: targets for chemotherapy
inferred← citeshttps://doi.org/10.1128/mbio.02129-25openalex-snapshot
Inhibition of the assembly of Plasmodium Hsp70-1 and Hsp40 complex blocks DNA replication by destabilizing ribonucleotide reductase subunit-2
inferred← citeshttps://doi.org/10.1155/2014/172582openalex-snapshot
Investigating the Chaperone Properties of a Novel Heat Shock Protein, Hsp70.c, fromTrypanosoma brucei
inferred← citeshttps://doi.org/10.1186/s13065-024-01159-6openalex-snapshot
Iso-mukaadial acetate and ursolic acid acetate bind to Plasmodium Falciparum heat shock protein 70: towards targeting parasite protein folding pathway
inferred← citeshttps://doi.org/10.1371/journal.pone.0121243openalex-snapshot
DnaK Protein Alleviates Toxicity Induced by Citrate-Coated Gold Nanoparticles in Escherichia coli
inferred← citeshttps://doi.org/10.1371/journal.pone.0129445openalex-snapshot
Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) Protein
inferred← citeshttps://doi.org/10.1371/journal.pone.0135326openalex-snapshot
Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand Selectivity
inferred← citeshttps://doi.org/10.1371/journal.pone.0148517openalex-snapshot
The Malarial Exported PFA0660w Is an Hsp40 Co-Chaperone of PfHsp70-x
inferred← citeshttps://doi.org/10.1371/journal.pone.0152626openalex-snapshot
Use of a Chimeric Hsp70 to Enhance the Quality of Recombinant Plasmodium falciparum S-Adenosylmethionine Decarboxylase Protein Produced in Escherichia coli
inferred← citeshttps://doi.org/10.1371/journal.pone.0226657openalex-snapshot
Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers
inferred← citeshttps://doi.org/10.1515/bc.2011.040openalex-snapshot
Screening for small molecule modulators of Hsp70 chaperone activity using protein aggregation suppression assays: inhibition of the plasmodial chaperone PfHsp70-1
inferred← citeshttps://doi.org/10.1515/hsz-2014-0138openalex-snapshot
Selective modulation of plasmodial Hsp70s by small molecules with antimalarial activity
inferred← citeshttps://doi.org/10.2174/138161213804143734openalex-snapshot
Hsp70s and J Proteins of Plasmodium Parasites Infecting Rodents and Primates: Structure, Function, Clinical Relevance, and Drug Targets
inferred← citeshttps://doi.org/10.2174/1570164615666180626123823openalex-snapshot
Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria andLeishmaniasis
inferred← citeshttps://doi.org/10.2174/187152610791163417openalex-snapshot
Malaria Heat Shock Proteins: Drug Targets that Chaperone other Drug Targets
inferred← citeshttps://doi.org/10.32657/10356/142305openalex-snapshot
Role of STEVOR and its interacting partners in parasite virulence
inferred← citeshttps://doi.org/10.3389/fmolb.2015.00034openalex-snapshot
Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle
inferred← citeshttps://doi.org/10.3389/fsufs.2026.1866725openalex-snapshot
A proteomic analysis of heat shock proteins from pigeonpea (Cajanus cajan) seed
inferred← citeshttps://doi.org/10.3390/biom10060856openalex-snapshot
Comparative Characterization of Plasmodium falciparum Hsp70-1 Relative to E. coli DnaK Reveals the Functional Specificity of the Parasite Chaperone
inferred← citeshttps://doi.org/10.3390/biom9100543openalex-snapshot
The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function
inferred← citeshttps://doi.org/10.3390/ijms20235930openalex-snapshot
Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites
inferred← citeshttps://doi.org/10.3390/ijms22042226openalex-snapshot
Mutation of GGMP Repeat Segments of Plasmodium falciparum Hsp70-1 Compromises Chaperone Function and Hop Co-Chaperone Binding
inferred← citeshttps://doi.org/10.3390/microorganisms13092195openalex-snapshot
Acanthospermum australe Extract Inhibits the Chaperone Activity of Plasmodium falciparum Heat Shock Protein 70-1
inferred← citeshttps://doi.org/10.3390/molecules22071224openalex-snapshot
Extracts Obtained from Pterocarpus angolensis DC and Ziziphus mucronata Exhibit Antiplasmodial Activity and Inhibit Heat Shock Protein 70 (Hsp70) Function
inferred← citeshttps://doi.org/10.3390/molecules22122139openalex-snapshot
(−)-Epigallocatechin-3-Gallate Inhibits the Chaperone Activity of Plasmodium falciparum Hsp70 Chaperones and Abrogates Their Association with Functional Partners
inferred← citeshttps://doi.org/10.5897/jmpr2015.5740openalex-snapshot
Anticoagulant and anti-inflammatory activity of a triterpene from Protorhus longifolia stem bark
inferred← citeshttps://doi.org/10.6084/m9.figshare.26695065openalex-snapshot
Additional file 1 of Iso-mukaadial acetate and ursolic acid acetate bind to Plasmodium Falciparum heat shock protein 70: towards targeting parasite protein folding pathway
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.